Search PubMed⌕ Search

Biomedical subjects

L Lin

Publications and source records attributed to L Lin.

At least 397 records · Page 22Linked to original sources

The introduction of postpartum intrauterine devices in the People's Republic of China.

In China, which has a commitment to family planning and, in particular, to the one-child family, a postpartum IUD should be widely accepted and could have significant impact on the Chinese family planning program. This report presents the introduction of the Delta T and Delta Loop devices, with 200 immediate postpartum insertions. Fifty-two deliveries were by cesarean section. The 6-month expulsion rates were 13.3 and 17.2 for the Delta T and Delta Loop, respectively. There was one pregnancy reported. Analysis suggests that the two devices are suitable for use in the postpartum period for Chinese women.

Adult↗

Evaluation of the preterm infant for patent ductus arteriosus.

As a first step in a multicenter, collaborative project to study the role of indomethacin in the management of patent ductus arteriosus in premature infants, a diagnostic scheme was developed, on an a priori basis, by a consensus of the participating neonatologists and pediatric cardiologists. The scheme, which utilizes clinical and noninvasive findings, was designed to detect infants with a "hemodynamically significant" patent ductus arteriosus (PDA). Among 1,689 infants with birth weight less than 1,750 g who were monitored during the first year of the study, 342 (20.2%) met the criteria for PDA. Rates were higher for smaller infants (42% with birth weight less than 1,000 g) than for larger infants (7% with birth weight 1,500 to 1,750 g). Although study protocol did not require a direct procedure to confirm the diagnosis of PDA, a marked decrease in the presence of most criteria was noted following surgical ligation of the ductus. Although the echocardiographic criterion (ratio of left atrium to aorta [LA/Ao] greater than or equal to 1.15) proved to have a low specificity for PDA, the data suggest that the overall scheme led to a very low rate of false-positive diagnosis. Following the application of the scheme for 1 year at 13 clinical centers, it has been shown to be a highly acceptable means of detecting infants with PDA.

Clinical Trials as Topic↗

Binkhorst Lecture (Part 1). Experimental cataract surgery.

The use of intraocular lenses in cataract surgery leads to a greater corneal complication rate than surgical treatment without such devices. It has been assumed that the predominant reason for this is surgical trauma at the time of lens insertion. A laboratory study to verify and analyze this difference has been carried out, the cat being used as an experimental model. This first report evaluates the effect of the usual steps of cataract extraction on the density of corneal endothelial cells.

Animals↗

Binkhorst Lecture. (Part 2). Experimental cataract surgery--electron microscopy.

Scanning and transmission electron microscopic examinations were performed on cat corneas after the steps usually taken to perform cataract extraction were completed. The endothelium did not replicate, but showed nuclear division or segmentation occasionally. In each case, the anterior segment was free from any evidence of inflammation one year after surgical treatment--unless a pseudophakos had been inserted: in some of these cases, significant numbers of white cells were present, a condition that may contribute to anterior segment complications from implants.

Animals↗

Increased reproductive fitness of Escherichia coli lambda lysogens.

Lambda lysogens of Escherichia coli reproduce more rapidly than nonlysogens during aerobic growth in glucose-limited chemostats. If the environment is changed to anaerobic growth, the situation is reversed, and the lysogen reproduces more slowly than the nonlysogen. Based on a tetrazolium dye assay, the increased fitness of the lambda lysogen during aerobic growth seems to result from a continued high metabolic rate as glucose becomes limiting, whereas the metabolic rate of the nonlysogen declines. The lambda rex gene is required for the growth advantage of lysogens since lack of rex function causes lambda lysogens to lose their reproductive advantage over nonlysogens.

Aerobiosis↗

Reproductive fitness of P1, P2, and Mu lysogens of Escherichia coli.

P1, P2, and Mu lysogens of Escherichia coli reproduce more rapidly than nonlysogens during aerobic growth in glucose-limited chemostats. Thus, prophage-containing stains of E. coli are reproductively more fit than the corresponding nonlysogens. If mixed populations are grown by serial dilution under conditions in which growth is not limited, both the lysogen and nonlysogen manifest identical growth rates. The increased fitness of the lysogens in glucose-limited chemostats correlates with a higher metabolic activity of the lysogen as compared with the nonlysogen during glucose exhaustion. We propose that P1, P2, Mu, and lambda prophage all confer an evolutionarily significant reproductive growth advantage to E. coli lysogenic strains.

Aerobiosis↗

Molecular alterations of interferons.

Interferons can be chemically and enzymatically altered to obtain molecular forms which differ in size, charge, and/or host-range from native interferons. These data suggest that small active cores of interferons can be obtained which may possess more desirable characteristics than native interferons, such as lack of "species-specificity"" and increased stabilities. Studies for assessing alterations of interferons due to chemical or enzymatic treatments must monitor the treated interferons for changes in ratios of each of the various activities attributed to native interferons and must characterize the altered interferons in terms of each of the physical and biological markers.

Animals↗

The carbamate reaction of glycylglycine, plasma, and tissue extracts evaluated by a pH stopped flow apparatus.

We have used a stopped flow rapid reaction pH apparatus to investigate the carbamate equilibrium in glycylglycine solutions and in three biological tissues, human plasma, sheep muscle, and sheep brain, as well as to investigate the kinetics of carbamate formation in glyclyglycine solution and in human plasma. The rapid reaction apparatus was equipped with a pH sensitive glass electrode in order to follow the time course of pH from 0.005 to 100 s after rapid mixing of a solution of amine or protein and CO2. Two phases of the pH curve were observed: a fast phase representing carbamate formation, and a slow phase due to the hydration of CO2 which was uncatalyzed since a carbonic anhydrase inhibitor was added to the biological solutions. From the time course of pH change during the fast phase K2, the R-NH2 ionization constant, and Kc, the carbamate equilibrium constant as well as the velocity constant for the formation of carbamate, ka could be calculated from data at different pH and pCO2. The carbamate formed in glycylglycine solutions over a wide range of pH and pCO2 was found consistent with the theory of carbamate formation and with published data. At ionic strength 0.16 and 37 degrees pK is 7.67. pKc 4.58. The heat of the carbamate reaction (deltaH) was calculated to be -3.2 kcal/mol between 20 degrees and 37 degrees. Kt of glycylglycine depends quantitatively on ionic strength as predicted by the Debye-Huckel theory. With ionic strength 0.16 ku was found to be 2,500 M1 S1 at 37 degrees. The activation energy of carbamate formation is 6.7 kcal/mol. Carbamate measurements in human plasma at pCO2 from 38 to 359 Torr. pH from 6.9 to 8.3, temperature 37 degrees, and ionic strength 0.15 provided evidence that two kinds of amino groups participate in carbamate formation. From the equilibrium constants computed for the two species they could be identified as alpha- and epsilon-amino groups. On the basis of a protein molecular weight of 69.000. 0.6 alpha-amino groups/molecule with pKz=7.0 and pKc=4.2, and 5.9 epsilon-amino groups/molecule with pKz=9.0 and pKc=4.3 contribute to carbamate formation. The velocity constant ka was estimated to be 4,950 M1 S1 for the alpha-amino groups and 13,800 M1 S1 for the epsilon-amino groups. Under physiological conditions (pCO2=40 Torr. pH=7.4). The concentration of carbamate in plasma is 0.6 mM and the half-time of carbamate formation is 0.05 s. In extracts prepared from sheep brain at 37 degrees pH=7 and pCO2=35 Torr. the carbamate formation was estimated to be 0.8 mM. With pCO2=70 Torr and the same pH and temperature the carbamate concentration in muscle approximates 0.3 mM and increases to 7 mM as pH rises to 8. It is concluded that, as in plasma, a considerable number of epsilon-amino groups appear to be available for carbamate formation in these tissues.

Animals↗

Binding interactions between radiolabeled Escherichia coli elongation factor G and the ribosome.

We have prepared homogeneous radiolabeled Escherichia coli Elongation Factor G (EF-G) and examined its interactions with the ribosome. In agreement with earlier indirect observations we found that in the presence of high concentrations of fusidic acid approximately equimolar amounts of [3H]EF-G and [alpha-32P]GDP are stably bound to the ribosome. In the absence of fusidic acid, we observed a previously undescribed nucleotide-independent binding interaction between EF-G and the ribosome. This binding is detectable by rapid elution on small gel columns but is not apparent when reactions are analyzed by sucrose density gradient sedimentation. With the exception of the fact that the nucleotide-independent binding of EF-G to ribosome is apparently unaffected even by high concentrations of fusidic acid, it shares many properties in common with that binding which occurs in the presence of GDP. Nucleotide-independent binding requires magnesium ion (10 to 20 mM ) and does not require a monovalent cation but is strongly inhibited by even moderate concentrations of NH4Cl. This binding requires the presence on the ribosome of Protein L7/L12 and is inhibited by the antibiotic thiostrepton. Although we were unable to examine the binary ribosome.EF-G complex by equilibrium means, the observed stoichiometry under the conditions we employed did not exceed 0.2 mol of EF-G/mole of ribosome. Nonequilibrium measurements revealed that one-half of the EF-G was bound at a ribosome concentration of about 50 muM.

Binding Sites↗